Journal article

Divalent Cations and Redox Conditions Regulate the Molecular Structure and Function of Visinin-Like Protein-1

Conan K Wang, Anne Simon, Christian M Jessen, Cristiano LP Oliveira, Lynsey Mack, Karl-Heinz Braunewell, James B Ames, Jan Skov Pedersen, Andreas Hofmann

PLoS One | PUBLIC LIBRARY SCIENCE | Published : 2011

Abstract

The NCS protein Visinin-like Protein 1 (VILIP-1) transduces calcium signals in the brain and serves as an effector of the non-retinal receptor guanylyl cyclases (GCs) GC-A and GC-B, and nicotinic acetyl choline receptors (nAchR). Analysis of the quaternary structure of VILIP-1 in solution reveals the existence of monomeric and dimeric species, the relative contents of which are affected but not exclusively regulated by divalent metal ions and Redox conditions. Using small-angle X-ray scattering, we have investigated the low resolution structure of the calcium-bound VILIP-1 dimer under reducing conditions. Scattering profiles for samples with high monomeric and dimeric contents have been obta..

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University of Melbourne Researchers

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Awarded by National Institutes of Health


Awarded by National Health and Medical Research Council


Awarded by NATIONAL EYE INSTITUTE


Funding Acknowledgements

This work was supported in parts by Fundacao Bial, the Rebecca Cooper Foundation (AH), and National Institutes of Health (grant EY012347, J.B.A.). C. W. is supported by an National Health and Medical Research Council postdoctoral training fellowship (37677). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. No additional external funding received for this study.